Stabilizing and destabilizing effects of placing beta-branched amino acids in protein alpha-helices.

doi:10.1021/bi00206a003

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Article

Stabilizing and destabilizing effects of placing beta-branched amino acids in protein alpha-helices.

Biochemistry - 11 Oct 1994

Cornish V W, Kaplan M I, Veenstra D L, Kollman P A, Schultz P G

Abstract excerpt

In order to gain greater insight into the effects of beta-branched amino acids on protein alpha-helices, hydrophobic amino acids with varying degrees of beta-branching, including the fully beta-substituted L-2-amino-3,3-dimethylbutanoic acid (ADBA), were incorporated into the protein T4 lysozyme. The unnatural and natural amino acids were substituted at two solvent-exposed alpha-helical sites, Ser 44 and Asn 68,...

Topics

Acetonitriles
Amino Acids, Branched-Chain
Asparagine
Bacteriophage T4
Base Sequence
Circular Dichroism
Computer Simulation
Drug Stability
Electrophoresis, Polyacrylamide Gel
Leucine
Magnetic Resonance Spectroscopy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Models, Molecular

Molecular Sequence Data

Muramidase

Mutation

Oligonucleotides

Protein Structure, Secondary

Serine

Source

Open in PubMed

Identifiers

PMID: 7918421
DOI: 10.1021/bi00206a003

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7918421-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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